ID   HISX1_ANAVT             Reviewed;         431 AA.
AC   Q3MEV7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Histidinol dehydrogenase 1;
DE            Short=HDH 1;
DE            EC=1.1.1.23;
GN   Name=hisD1; OrderedLocusNames=Ava_0855;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC       histidinol to L-histidinaldehyde and then to L-histidine (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: L-histidinol + 2 NAD(+) = L-histidine + 2
CC       NADH.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
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DR   EMBL; CP000117; ABA20479.1; -; Genomic_DNA.
DR   RefSeq; YP_321374.1; -.
DR   GeneID; 3681756; -.
DR   GenomeReviews; CP000117_GR; Ava_0855.
DR   KEGG; ava:Ava_0855; -.
DR   NMPDR; fig|240292.3.peg.61; -.
DR   HOGENOM; Q3MEV7; -.
DR   OMA; Q3MEV7; YGIGMKK.
DR   BioCyc; AVAR240292:AVA_0855-MON; -.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01024; -; 1.
DR   InterPro; IPR001692; Histidinol_DH_CS.
DR   InterPro; IPR012131; Hstdl_DH_prok-type.
DR   PANTHER; PTHR21256:SF2; Hstdl_DH_prok; 1.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   ProDom; PD002680; Histidinol_dh; 1.
DR   TIGRFAMs; TIGR00069; hisD; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis;
KW   Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN         1    431       Histidinol dehydrogenase 1.
FT                                /FTId=PRO_0000229848.
FT   ACT_SITE    324    324       Proton acceptor (By similarity).
FT   ACT_SITE    325    325       Proton acceptor (By similarity).
FT   METAL       256    256       Zinc (By similarity).
FT   METAL       259    259       Zinc (By similarity).
FT   METAL       358    358       Zinc (By similarity).
FT   METAL       417    417       Zinc (By similarity).
FT   BINDING     127    127       NAD (By similarity).
FT   BINDING     188    188       NAD (By similarity).
FT   BINDING     211    211       NAD (By similarity).
FT   BINDING     234    234       Substrate (By similarity).
FT   BINDING     256    256       Substrate (By similarity).
FT   BINDING     259    259       Substrate (By similarity).
FT   BINDING     325    325       Substrate (By similarity).
FT   BINDING     358    358       Substrate (By similarity).
FT   BINDING     412    412       Substrate (By similarity).
FT   BINDING     417    417       Substrate (By similarity).
SQ   SEQUENCE   431 AA;  45806 MW;  D3AC6AF531ED1B1A CRC64;
     MLVLKTTDQE FSTRFQSLVS DRREATVDVS GTVRDILAHV KAHGDAAVQE YTSRFDHYSP
     HSHHLSAAFI AEQAAKCSAE VKAAIELAAE RISSFHQKQL PQDIGYTDTV GVKLGLNWVA
     LSQVGIYVPG GRASYPSSVL MNALPAKIAG VERIVMTVPM PHGEINPAVL AAAQVAGVTE
     IYSIGGAQAV GALAYGTETI TPVDKIVGPG NAYVAEAKRQ VFGTVGIDSI AGPSEILVVA
     DRQNNPEWIA WDLLSQAEHD PSAQSILITD SESFAQQVIG AVEQILTTLP TTKVASSSWQ
     NHGAVIIVRD LAESIPLLNQ LAPEHVELCV DNPQLLASQI KCAGSLFLGR YTPEAIGDYL
     GGPNHVLPTS RSARFASGLS VYDFLKRITY LECNQAALQA IGQSAVTLAE TEGLPAHAGS
     VAVRLQGLND M
//